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Title: Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization

Abstract

Here, polybasic helical peptides, such as peptide p5, bind human amyloid extracts and synthetic amyloid fibrils. When radio labeled, peptide p5 has been shown to specifically bind amyloid in vivo thereby allowing imaging of the disease. Structural requirements for heparin and amyloid binding have been studied using analogues of p5 that modify helicity and chirality.

Authors:
 [1];  [1];  [1];  [1];  [2];  [1];  [1]
  1. Univ. of Tennessee, Knoxville, TN (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE; Work for Others (WFO)
OSTI Identifier:
1327690
Grant/Contract Number:
AC05-00OR22725
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biochemistry and Biophysics Reports
Additional Journal Information:
Journal Volume: 8; Journal Issue: C; Journal ID: ISSN 2405-5808
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; polybasic peptides; amyloid binding; heparin; amino acid spacing; CD; molecular dynamics

Citation Formats

Wall, Jonathan S., Williams, Angela, Wooliver, Craig, Martin, Emily B., Cheng, Xiaolin, Heidel, R. Eric, and Kennel, Stephen J.. Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization. United States: N. p., 2016. Web. doi:10.1016/j.bbrep.2016.08.007.
Wall, Jonathan S., Williams, Angela, Wooliver, Craig, Martin, Emily B., Cheng, Xiaolin, Heidel, R. Eric, & Kennel, Stephen J.. Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization. United States. doi:10.1016/j.bbrep.2016.08.007.
Wall, Jonathan S., Williams, Angela, Wooliver, Craig, Martin, Emily B., Cheng, Xiaolin, Heidel, R. Eric, and Kennel, Stephen J.. Thu . "Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization". United States. doi:10.1016/j.bbrep.2016.08.007. https://www.osti.gov/servlets/purl/1327690.
@article{osti_1327690,
title = {Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization},
author = {Wall, Jonathan S. and Williams, Angela and Wooliver, Craig and Martin, Emily B. and Cheng, Xiaolin and Heidel, R. Eric and Kennel, Stephen J.},
abstractNote = {Here, polybasic helical peptides, such as peptide p5, bind human amyloid extracts and synthetic amyloid fibrils. When radio labeled, peptide p5 has been shown to specifically bind amyloid in vivo thereby allowing imaging of the disease. Structural requirements for heparin and amyloid binding have been studied using analogues of p5 that modify helicity and chirality.},
doi = {10.1016/j.bbrep.2016.08.007},
journal = {Biochemistry and Biophysics Reports},
number = C,
volume = 8,
place = {United States},
year = {Thu Aug 11 00:00:00 EDT 2016},
month = {Thu Aug 11 00:00:00 EDT 2016}
}

Journal Article:
Free Publicly Available Full Text
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